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Breakthrough in methane research: How microbes can save our climate!
Researchers at the TU Berlin and the University of Marburg achieve a breakthrough with methyl coenzyme M reductase. Results published in “Nature”.
Breakthrough in methane research: How microbes can save our climate!
Researchers at the Center for Synthetic Microbiology (SYNMIKRO) at the Philipps University of Marburg and the TU Berlin have made significant progress in understanding methyl-coenzyme M reductase (MCR). This enzyme plays an essential role in biological methane production and is one of the most abundant enzymes on Earth. The results of this research were published in the renowned journal Nature and show a remarkable evolutionary connection to nitrogen fixation processes that are central to the global nitrogen cycle, as microorganisms absorb and convert nitrogen from the air. Loud TU Berlin This breakthrough is crucial to better address the challenges in the energy sector and climate change.
Dr. Christian Lorent, a co-author of the study, highlights that up to a billion tons of methane are produced annually by methanogenic archaea. These emissions contribute to global warming, but also offer potential as a renewable energy source. MCR is responsible for producing methane in a complex biochemical process, and the research team isolated and characterized the MCR activation complex from Methanococcus maripaludis. It also identified a significant influence of a small protein called McrC, which activates MCR in an ATP-dependent process. This discovery deepens our understanding of the molecular mechanisms underlying methane production.
The role of MCR in methanogenesis
MCR catalyzes the final step of methanogenesis and also plays a crucial role in the anaerobic oxidation of methane. The structure of MCR includes a unique nickel tetrahydrocorphinoid, also known as coenzyme F430, and various unusual post-translational modifications (PTMs). These modifications are crucial for the function of the enzyme, which occurs in methanogenic archaea as two isoenzymes (MCRI and MCRII). A new type, MCRIII, was identified in Methanococcales. However, few studies have been conducted on these modifications to date. Highlighted in a comprehensive overview of current knowledge of MCR and its PTMs PMCID that future research is needed to better understand the functions of PTMs and their influence on MCR activity and stability.
The active site of MCR contains coenzyme F430, whose nickel ion catalyzes necessary redox reactions in the Ni(1+) oxidation state. The reaction mechanisms at the active site involve two substrates and produce methane and other products, with three possible mechanisms for this reaction being investigated. These findings are important not only for basic research, but also for the development of new technologies for generating energy from biological sources.
The discovery of the three specialized metal complexes required for the activation mechanism of MCR shows parallels to the catalysts found in nitrogenase. The similarity between these systems suggests that there may be a common evolutionary origin, highlighting the general complexity and adaptability of biological catalysts. Dr. Lorent therefore calls for research into natural catalysts for energy production and climate protection to be intensified.